Structure of PDB 1ish Chain A Binding Site BS01

Receptor Information
>1ish Chain A (length=250) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
WRAEGTSAHLRDIFLGRCAEYRALLSPEQRNKDCTAIWEAFKVALDKDPC
SVLPSDYDLFITLSRHSIPRDKSLFWENSHLLVNSFADNTRRFMPLSDVL
YGRVADFLSWCRQKADSGLDYQSCPTSEDCENNPVDSFWKRASIQYSKDS
SGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGP
NVESCGEGSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALK
Ligand information
Ligand IDENP
InChIInChI=1S/C17H24N5O17P3/c23-10-7(37-17(26)12(10)25)3-34-41(30,31)39-42(32,33)35-4-8-11(24)13(38-40(27,28)29)16(36-8)22-6-19-9-14-18-1-2-21(14)5-20-15(9)22/h1-2,5-8,10-13,16-17,23-26H,3-4H2,(H,30,31)(H,32,33)(H2,27,28,29)/t7-,8-,10-,11-,12-,13-,16-,17-/m1/s1
InChIKeyKWEQFQACRLGUSH-QJWJOKBXSA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[C@@H]1O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]2O[C@H]([C@H](O[P](O)(O)=O)[C@@H]2O)n3cnc4c5nccn5cnc34)[C@@H](O)[C@H]1O
OpenEye OEToolkits 1.5.0c1cn2cnc3c(c2n1)ncn3[C@H]4[C@@H]([C@@H]([C@H](O4)CO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]5[C@H]([C@H]([C@@H](O5)O)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0c1cn2cnc3c(c2n1)ncn3C4C(C(C(O4)COP(=O)(O)OP(=O)(O)OCC5C(C(C(O5)O)O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH]1O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O[P](O)(O)=O)[CH]2O)n3cnc4c5nccn5cnc34)[CH](O)[CH]1O
ACDLabs 10.04O=P(O)(O)OC4C(O)C(OC4n2c3ncn1ccnc1c3nc2)COP(=O)(O)OP(=O)(O)OCC5OC(O)C(O)C5O
FormulaC17 H24 N5 O17 P3
NameETHENO-NADP
ChEMBL
DrugBankDB03732
ZINCZINC000024631640
PDB chain1ish Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ish Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		F76 W77 E78 H81 L97 A106 D107 F108 L109 W111 W140 S144 F173 F174 E178
Binding residue
(residue number reindexed from 1)		F75 W76 E77 H80 L96 A105 D106 F107 L108 W110 W139 S143 F172 F173 E177
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) S98 F173 E178
Catalytic site (residue number reindexed from 1) S97 F172 E177
Enzyme Commision number 3.2.2.6: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
Gene Ontology
Molecular Function
GO:0003953 NAD+ nucleosidase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016849 phosphorus-oxygen lyase activity
GO:0061809 NAD+ nucleotidase, cyclic ADP-ribose generating
Biological Process
GO:0001952 regulation of cell-matrix adhesion
GO:0002691 regulation of cellular extravasation
GO:0006959 humoral immune response
GO:0007165 signal transduction
GO:0008284 positive regulation of cell population proliferation
GO:0030890 positive regulation of B cell proliferation
GO:0032956 regulation of actin cytoskeleton organization
GO:0050727 regulation of inflammatory response
GO:0050730 regulation of peptidyl-tyrosine phosphorylation
GO:0050848 regulation of calcium-mediated signaling
GO:0090022 regulation of neutrophil chemotaxis
GO:0090322 regulation of superoxide metabolic process
GO:2001044 regulation of integrin-mediated signaling pathway
Cellular Component
GO:0001931 uropod
GO:0005576 extracellular region
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0035579 specific granule membrane
GO:0070062 extracellular exosome
GO:0098552 side of membrane

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ish, PDBe:1ish, PDBj:1ish
PDBsum1ish
PubMed11866528
UniProtQ10588|BST1_HUMAN ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (Gene Name=BST1)

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